ArticlebioRxiv : the preprint server for biology2026
Zinc Differentially Modulates Tau Aggregation, Fibril Morphology, and Prion-like Seeding in a Construct-Dependent Manner.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
The role of tau fibril structure in seeding and propagation of aggregation remains a central unresolved question in tauopathy biology. While non-proteinaceous cofactors are increasingly observed in patient-derived tau filaments, whether they actively determine fibril structure and function is not well understood. Here, we show that zinc, a divalent cation dysregulated in Alzheimer's disease (AD), can drive fundamentally different aggregation and seeding outcomes depending on tau sequence context. Using heparin-free conditions, we compared full-length 2N4R tau (residues 1-441) with an AD-tau fragment (residues 304-380) corresponding to the ordered fibril core. Strikingly, Zn
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